Department of Biophysical Chemistry, Kyoto Pharmaceutical University, Yamashina-ku, Kyoto, Japan.
Mol Biol Rep. 2010 Mar;37(3):1165-8. doi: 10.1007/s11033-009-9477-7. Epub 2009 Mar 5.
Nubp1 (also known as Nbp35) and Nubp2 (also known as Cfd1) proteins are known to be responsible for regulating centrosome duplication in mouse and ribosome biogenesis in yeast. Nubp proteins contribute to diverse physiological functions. It is thought that Nubp1 and Nubp2 proteins interact with each other and regulate their functions. However, little is known about the intracellular localization of Nubp proteins. In this study, we compared the intracellular localization of human Nubp1 and Nubp2 by fusing these proteins with green fluorescent protein (GFP) in HeLa cells. The nuclear transfer of Nubp1-GFP, where GFP was fused to the C-terminus, was not observed. However, GFP-Nubp1, where GFP was fused to the N-terminus, did accumulate in the nucleus. In addition, GFP-modification at the N-terminal of Nubp2 induced nuclear transformation. Our data suggest that the C-terminal region of Nubp1 is important for nuclear transfer and the N-terminal of Nubp2 contributes to the morphology of the nucleus.
Nubp1（也称为 Nbp35）和 Nubp2（也称为 Cfd1）蛋白已知负责调节小鼠中心体复制和酵母核糖体生物发生。Nubp 蛋白有助于多种生理功能。据认为，Nubp1 和 Nubp2 蛋白相互作用并调节其功能。然而，关于 Nubp 蛋白的细胞内定位知之甚少。在这项研究中，我们通过将这些蛋白与绿色荧光蛋白（GFP）融合在 HeLa 细胞中来比较人 Nubp1 和 Nubp2 的细胞内定位。未观察到 GFP 融合到 C 末端的 Nubp1-GFP 的核转移。然而，GFP-Nubp1，其中 GFP 融合到 N 末端，确实在核内积累。此外，Nubp2 的 N 末端的 GFP 修饰诱导核转化。我们的数据表明，Nubp1 的 C 末端区域对于核转移很重要，而 Nubp2 的 N 末端有助于核的形态。
